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1. Mutagenesis of human profilin locates its poly(L-proline)-binding site to a hydrophobic patch of aromatic amino acids.

Author

Björkegren C, Rozycki M, Schutt CE, Lindberg U, and Karlsson R

Subjects
Amino Acids chemistry, Amino Acids metabolism, Binding Sites, Humans, Microfilament Proteins genetics, Microfilament Proteins metabolism, Mutagenesis, Profilins, Recombinant Proteins chemistry, Recombinant Proteins metabolism, Saccharomyces cerevisiae, Contractile Proteins, Microfilament Proteins chemistry, Peptides metabolism
Abstract

The actin-binding protein, profilin, contains a src-homology (SH) 3-like fold (Schutt, C.E. et al., submitted), and its tight interaction with poly(L-proline) is reminiscent of the binding activity exhibited by SH3-domains. Here we demonstrate that replacements of aromatic amino acids in a hydrophobic patch on the surface of the profilin molecule abolish its poly(L-proline)-binding capacity. However, the location of this hydrophobic patch is found in another region of the molecule than that displaying structural similarities with SH3 domains.

Published
1993
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